Mark A. Brooks
University of Paris-Sud
17 Papers
148 Citations
Mark A. Brooks is an academic researcher from University of Paris-Sud. The author has contributed to research in topics: Protein structure & RNA. The author has an hindex of 12, co-authored 17 publications. Previous affiliations of Mark A. Brooks include University of Leeds & Centre national de la recherche scientifique.
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Papers
Binding Mode and Structure-Activity Relationships around Direct Inhibitors of the Nrf2-Keap1 Complex.
Eric Jnoff,Claudia Albrecht,John J. Barker,Oliver Barker,Edward Beaumont,Steven Bromidge,Frederick Arthur Brookfield,Mark A. Brooks,Christian Bubert,Tom Ceska,Vincent Anthony Corden,Graham Dawson,Stephanie Duclos,Tara Fryatt,Christophe Genicot,Emilie Jigorel,Jason Kwong,Rosemary Maghames,Innocent Mushi,Richard Pike,Zara A. Sands,Myron A. Smith,Christopher C. Stimson,Jean-Philippe Courade +23 more
TL;DR: This X‐ray crystal structure provides breakthrough experimental evidence for the true binding mode of the hit compound (S,R,S)‐1 a, as the ligand orientation was found to differ from that of the initial docking model, which was available at the start of the project.
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Structure of the yeast Pml1 splicing factor and its integration into the RES complex.
Mark A. Brooks,Andrzej Dziembowski,Sophie Quevillon-Cheruel,Véronique Henriot,Céline Faux,Herman van Tilbeurgh,Bertrand Séraphin +6 more
TL;DR: It is shown that mutation of the putative phosphothreonine-binding pocket of Pml1 does not affect pre-mRNA splicing, and a model of the organization of the RES complex is proposed based on these results, and the functional consequences of this architecture are discussed.
The structure of an archaeal homodimeric ligase which has RNA circularization activity.
Mark A. Brooks,Laurence Meslet-Cladiere,Marc Graille,Joëlle Kuhn,Karine Blondeau,Hannu Myllykallio,Herman van Tilbeurgh +6 more
TL;DR: The structure of Pab1020 in complex with the ATP analog AMPPNP is solved by single‐wavelength anomalous dispersion (SAD), elucidating a structure with high structural similarity to the catalytic domains of two RNA ligases from the bacteriophage T4.
X-Ray Structure and Site-Directed Mutagenesis Analysis of the Escherichia coli Colicin M Immunity Protein
Fabien Gérard,Fabien Gérard,Mark A. Brooks,Mark A. Brooks,Hélène Barreteau,Hélène Barreteau,Thierry Touzé,Thierry Touzé,Marc Graille,Marc Graille,Ahmed Bouhss,Ahmed Bouhss,Didier Blanot,Didier Blanot,Herman van Tilbeurgh,Herman van Tilbeurgh,Dominique Mengin-Lecreulx,Dominique Mengin-Lecreulx +17 more
TL;DR: The resolution of the crystal structure of Cmi revealed a disulfide bond between residues Cys31 and Cys107, which appeared to be conserved in the sequences of several proteins of unknown function belonging to the YebF family which exhibit 25 to 35% overall sequence similarity with Cmi.
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Structure-based discovery of LpxC inhibitors
Jing Zhang,Audrey Chan,Lippa Blaise S,Jason B. Cross,Liu Christopher Matthew,Ning Yin,Jan Antoinette C. Romero,Jonathan F. Lawrence,Ryan Heney,Prudencio S. Herradura,Jennifer Goss,Cynthia Clark,Cassandra Abel,Yanzhi Zhang,Katherine M. Poutsiaka,Felix Epie,Mary Conrad,Azard Mahamoon,Kien T. Nguyen,Ajit Chavan,Edward Clark,Tongchuan Li,Robert K. Y. Cheng,Michael W. Wood,Ole A. Andersen,Mark A. Brooks,Jason Kwong,John M. Barker,Ian Parr,Yugui Gu,M. Dominic Ryan,Scott Coleman,Chester A. Metcalf +32 more
TL;DR: The efforts toward the discovery of novel LpxC inhibitors are presented herein and it is shown that novel antimicrobials that could overcome the resistance problems are urgently needed.
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